人β-副肌球蛋白的溶液结构及其与旁系同源物α-副肌球蛋白和大鼠直系同源物的结构比较。

Solution structure of human beta-parvalbumin and structural comparison with its paralog alpha-parvalbumin and with their rat orthologs.

作者信息

Babini Elena, Bertini Ivano, Capozzi Francesco, Del Bianco Cristina, Hollender Dominik, Kiss Tamas, Luchinat Claudio, Quattrone Alessandro

机构信息

CERM, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy.

出版信息

Biochemistry. 2004 Dec 28;43(51):16076-85. doi: 10.1021/bi048388o.

DOI:10.1021/bi048388o

PMID:15610002

Abstract

The aim of this research was to determine the structure of human beta-parvalbumin (109 amino acids) and to compare it with its paralog and ortholog proteins. The structure was determined in solution using multinuclear and multidimensional NMR methods and refined using substitution of the EF-hand Ca(2+) ion with a paramagnetic lanthanide. The resulting family of structures had a backbone rmsd of 0.50 A. Comparison with rat oncomodulin (X-ray, 1.3 A resolution) as well as with human (NMR, backbone rmsd of 0.49 A) and rat (X-ray, 2.0 A resolution) parvalbumins reveals small but reliable local differences, often but not always related to amino acid variability. The analysis of these structures has led us to propose an explanation for the different affinity for Ca(2+) between alpha- and beta-parvalbumins and between parvalbumins and calmodulins.

摘要

本研究的目的是确定人β-小白蛋白（109个氨基酸）的结构，并将其与其旁系同源蛋白和直系同源蛋白进行比较。该结构通过多核和多维核磁共振方法在溶液中测定，并通过用顺磁性镧系元素取代EF-手型Ca(2+)离子进行优化。所得的结构家族的主链均方根偏差为0.50 Å。与大鼠癌调蛋白（X射线，分辨率1.3 Å）以及与人（核磁共振，主链均方根偏差0.49 Å）和大鼠（X射线，分辨率2.0 Å）小白蛋白的比较揭示了微小但可靠的局部差异，这些差异通常但并非总是与氨基酸变异性有关。对这些结构的分析使我们能够对α-和β-小白蛋白之间以及小白蛋白和钙调蛋白之间对Ca(2+)的不同亲和力提出一种解释。